BCAS3_MOUSE
ID BCAS3_MOUSE Reviewed; 928 AA.
AC Q8CCN5; Q8CC16; Q9EPX3;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=BCAS3 microtubule associated cell migration factor;
DE AltName: Full=Breast carcinoma-amplified sequence 3 homolog {ECO:0000250|UniProtKB:Q9H6U6};
DE AltName: Full=K20D4 {ECO:0000303|PubMed:16099728};
DE AltName: Full=Protein rudhira {ECO:0000303|PubMed:16099728};
GN Name=Bcas3 {ECO:0000250|UniProtKB:Q9H6U6, ECO:0000312|MGI:MGI:2385848};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-477 (ISOFORM 1), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=16099728; DOI=10.1016/j.modgep.2005.06.002;
RA Siva K., Inamdar M.S.;
RT "Rudhira is a cytoplasmic WD40 protein expressed in mouse embryonic stem
RT cells and during embryonic erythropoiesis.";
RL Gene Expr. Patterns 6:225-234(2006).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [4]
RP ERRATUM OF PUBMED:16617102.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [5]
RP INDUCTION, AND CHROMATIN-BINDING.
RX PubMed=17505058; DOI=10.1210/me.2006-0514;
RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
RT coactivator, through proline-, glutamic acid-, and leucine-rich protein-1
RT (PELP1).";
RL Mol. Endocrinol. 21:1847-1860(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-480; SER-488;
RP SER-838; SER-886 AND SER-898, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22300583; DOI=10.1016/j.yexcr.2012.01.016;
RA Jain M., Bhat G.P., Vijayra havan K., Inamdar M.S.;
RT "Rudhira/BCAS3 is a cytoskeletal protein that controls Cdc42 activation and
RT directional cell migration during angiogenesis.";
RL Exp. Cell Res. 318:753-767(2012).
CC -!- FUNCTION: Functions synergistically with PELP1 as a transcriptional
CC coactivator of estrogen receptor-responsive genes. Stimulates histone
CC acetyltransferase activity. Binds to chromatin (By similarity). Plays a
CC role in angiogenesis. Participates in the regulation of cell polarity
CC and directional endothelial cell migration by mediating both the
CC activation and recruitment of CDC42 and the reorganization of the actin
CC cytoskeleton at the cell leading edge. Promotes filipodia formation.
CC Plays a regulatory role in autophagic activity. In complex with PHAF1,
CC associates with the preautophagosomal structure during both non-
CC selective and selective autophagy. Probably binds phosphatidylinositol
CC 3-phosphate (PtdIns3P) which would mediate the recruitment
CC preautophagosomal structures (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}.
CC -!- SUBUNIT: Interacts with histone H3, ESR1, KAT2B and PELP1; the
CC interactions occur in a estrogen-dependent manner. Interacts with beta-
CC tubulin and VIM. Interacts (via C-terminal) with PHAF1; the interaction
CC is requrired for the association with the phagophore (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6U6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6U6}. Cytoplasm
CC {ECO:0000269|PubMed:16099728, ECO:0000269|PubMed:22300583}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:22300583}. Preautophagosomal structure
CC {ECO:0000250|UniProtKB:Q9H6U6}. Note=Associates with chromatin.
CC Recruited to estrogen receptor-induced promoters in a PELP1-dependent
CC manner (By similarity). Localizes in the cytoplasm in stationary cells.
CC Translocates from the cytoplasm to the leading edge in motile cells.
CC Colocalizes with microtubules and intermediate filaments in both
CC stationary and motile cells. The BCAS3:PHAF1 complex is recruited to
CC the preautophagosomal structures adjacent to the damaged mitochondria
CC upon mitophagy in a PRKN-PINK1 dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9H6U6, ECO:0000269|PubMed:22300583}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CCN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCN5-2; Sequence=VSP_007861, VSP_007862;
CC -!- TISSUE SPECIFICITY: Expressed in blood islands and yolk sac blood
CC islands (at protein level). Highly expressed in mammary tumors.
CC Expressed in eostrogen-induced epithelial cells of mammary glands.
CC Expressed in brain, heart, kidney, lung, liver and spleen. Expressed in
CC embryonic stem cells, embryoid bodies, endothelial cells and
CC fibroblasts. {ECO:0000269|PubMed:16099728, ECO:0000269|PubMed:16617102,
CC ECO:0000269|PubMed:17505058}.
CC -!- DEVELOPMENTAL STAGE: Expressed in erythroid cells in the vessels at 9.5
CC and 10.5 dpc (at protein level). Expressed in embryo at 7.5 dpc and in
CC the yolk sac at 10.5 dpc. Expressed in the heart and yolk sac mesoderm
CC at 8.5 dpc. Expressed in the head mesenchyme, somitic mesoderm, otic
CC vesicle, vessels and few blood cells at 9.5 to 11.5 dpc.
CC {ECO:0000269|PubMed:16099728}.
CC -!- INDUCTION: Up-regulated by PELP1 in response to estrogen.
CC {ECO:0000269|PubMed:17505058}.
CC -!- DOMAIN: Has been proposed to contain 7 WD repeats. This prediction
CC could not be reproduced. {ECO:0000305|PubMed:16099728}.
CC -!- MISCELLANEOUS: 'Rudhira' stands for 'blood' in Sanskrit as this protein
CC is strongly expressed in blood vessels. {ECO:0000269|PubMed:16099728}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to an intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BCAS3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG34697.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF313800; AAG34697.1; ALT_SEQ; mRNA.
DR EMBL; AK032423; BAC27862.1; -; mRNA.
DR EMBL; AK034117; BAC28592.1; -; mRNA.
DR CCDS; CCDS25195.1; -. [Q8CCN5-1]
DR RefSeq; NP_001160114.1; NM_001166642.1.
DR RefSeq; NP_619622.3; NM_138681.4. [Q8CCN5-1]
DR RefSeq; XP_006532603.1; XM_006532540.2. [Q8CCN5-1]
DR AlphaFoldDB; Q8CCN5; -.
DR BioGRID; 228674; 2.
DR STRING; 10090.ENSMUSP00000103696; -.
DR iPTMnet; Q8CCN5; -.
DR PhosphoSitePlus; Q8CCN5; -.
DR SwissPalm; Q8CCN5; -.
DR EPD; Q8CCN5; -.
DR jPOST; Q8CCN5; -.
DR MaxQB; Q8CCN5; -.
DR PaxDb; Q8CCN5; -.
DR PeptideAtlas; Q8CCN5; -.
DR PRIDE; Q8CCN5; -.
DR ProteomicsDB; 273734; -. [Q8CCN5-1]
DR ProteomicsDB; 273735; -. [Q8CCN5-2]
DR Antibodypedia; 9303; 231 antibodies from 36 providers.
DR Ensembl; ENSMUST00000074875; ENSMUSP00000074416; ENSMUSG00000059439. [Q8CCN5-1]
DR Ensembl; ENSMUST00000108056; ENSMUSP00000103691; ENSMUSG00000059439. [Q8CCN5-2]
DR GeneID; 192197; -.
DR KEGG; mmu:192197; -.
DR UCSC; uc007krn.2; mouse. [Q8CCN5-2]
DR UCSC; uc007krp.2; mouse. [Q8CCN5-1]
DR CTD; 54828; -.
DR MGI; MGI:2385848; Bcas3.
DR VEuPathDB; HostDB:ENSMUSG00000059439; -.
DR eggNOG; KOG2109; Eukaryota.
DR eggNOG; KOG4415; Eukaryota.
DR GeneTree; ENSGT00390000006454; -.
DR HOGENOM; CLU_037675_0_0_1; -.
DR InParanoid; Q8CCN5; -.
DR OrthoDB; 537714at2759; -.
DR BioGRID-ORCS; 192197; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Bcas3; mouse.
DR PRO; PR:Q8CCN5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CCN5; protein.
DR Bgee; ENSMUSG00000059439; Expressed in seminal vesicle and 224 other tissues.
DR ExpressionAtlas; Q8CCN5; baseline and differential.
DR Genevisible; Q8CCN5; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0010698; F:acetyltransferase activator activity; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0035148; P:tube formation; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022175; BCAS3.
DR InterPro; IPR045142; BCAS3-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13268; PTHR13268; 1.
DR Pfam; PF12490; BCAS3; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Angiogenesis; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..928
FT /note="BCAS3 microtubule associated cell migration factor"
FT /id="PRO_0000050884"
FT REGION 254..312
FT /note="Required for recruitment to preautophagosomal
FT structure in response to mitophagy"
FT /evidence="ECO:0000250|UniProtKB:Q9H6U6"
FT REGION 437..560
FT /note="Required for recruitment to preautophagosomal
FT structure in response to mitophagy"
FT /evidence="ECO:0000250|UniProtKB:Q9H6U6"
FT REGION 472..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6U6"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H6U6"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H6U6"
FT VAR_SEQ 498..527
FT /note="LTSQDSYNNFTNNNPGNPRLSPLPSLMVVT -> HFPLMLLSSRFLLYHLGS
FT DANFYSVCAEHS (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT /id="VSP_007861"
FT VAR_SEQ 528..928
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT /id="VSP_007862"
FT CONFLICT 75
FT /note="R -> Q (in Ref. 1; BAC27862)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="T -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 101021 MW; EF8FE46CF7011A7B CRC64;
MNETMATDSP RRPSRCTGGV VVRPQAVTEQ SYMESVVTFL QDVVPQAYSG SPLTEEKEKI
VWVRFENADL NDTSRNLEFH ELHSTGNEPP LLVMIGYSDG MQVWGIPISG EAQELFSVRH
GPVRAARILP APQLGAQKCD NFAEKRPLLG VCKSIGSSGT TPPYCCVDLY SLRTGEMVKS
IQFKTPIYDL HCNKRILVVV LQEKIAAFDS CTFTKKFFVT SCYPCPGPNM NPIALGSRWL
AYAENKLIRC HQSRGGACGD NIQSYTATVL SAAKTLKSGL TMVGKVVTQL TGTLPSGVTE
DDVALHCNSR RSPLVPGIIT VIDTETVGEG QVLVSEDSDS DGIVAHFPAH EKPVCCMAFN
TSGMLLVTTD TLGHDFHVFQ ILTHPWSSSQ CAVHHLYTLH RGETEAKVQD ICFSHDCRWV
VVSTLRGTSH VFPINPYGGQ PCVRTHMSPR VVNRMSRFQK SAGLEEIEQE LTSKQGGRCS
PVPGLSSSPS GSPLHGKLTS QDSYNNFTNN NPGNPRLSPL PSLMVVTPLA QIKQPMTLGT
ITKRTGPYLF GAGCFSIKAP CKVKSPPQIS PSKSMGGEFC VAAVFGTSRS WFANNAGLKR
EKDQSKQVVV ESLYIISCYG TLVEHMIEPR PISTAPKISD DTPLEIMTSP RASWTLVRTP
QWNELQPPFN ANHPLLLAAE AVQYYQLLLA GSLPPGSPGP ITRHGSYDSL ASDHSGQEDE
EWLSQVEIVT HTGPHRRLWM GPQFHFKTIQ TSGQTTVIST SSSVLQSHGP SDTPQPLLDF
DTDDLDLNSL RIQPVRSDPV SMPGSSRAVS DRRGVSTVTD AASGTFDRSV TLLEVCGSWP
EGFGLRHMSS MEHSEEGLRE RLADAMAESP SRDVVGSGTE LQREGSIETL SNSSGSTSGS
IPRNFDGYRS PLPTNESQPL SLFPTGFP
